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ACTIVITY CRITICAL RESIDUE [1 record]
Record 1 - internal organization data 2011-01-05
Record 1, English
Record 1, Subject field(s)
- Biological Sciences
Record 1, Main entry term, English
- catalytic residue
1, record 1, English, catalytic%20residue
correct
Record 1, Abbreviations, English
Record 1, Synonyms, English
- activity critical residue 1, record 1, English, activity%20critical%20residue
correct
Record 1, Textual support, English
Record number: 1, Textual support number: 1 DEF
Amino acid residue directly involved in the covalent bond changes during enzyme action. 2, record 1, English, - catalytic%20residue
Record number: 1, Textual support number: 1 CONT
Chymotrypsinogen has a single polypeptide chain of 245 residues held together by five intrachain disulfide bridges... It is converted into active [alpha] chymotrypsin by the enzymatic hydrolysis of four peptide linkages, by sequential action of trypsin and chymotrypsin, with the release of two dipeptides. The active [alpha] chymotrypsin produced this way consists of three polypeptide chains held together by two -S-S bonds. Thus the two specific residues essential for catalytic activity, histidine 57 and serine 195, are present in two different chains. However, it has been directly established by x-ray analysis of the tertiary structure of chymotrypsin that these ... catalytic residues ... are actually very close to each other in the conformation of the native enzyme. 1, record 1, English, - catalytic%20residue
Record 1, French
Record 1, Domaine(s)
- Sciences biologiques
Record 1, Main entry term, French
- résidu catalytique
1, record 1, French, r%C3%A9sidu%20catalytique
correct, masculine noun
Record 1, Abbreviations, French
Record 1, Synonyms, French
- aminoacide catalytiquement actif 2, record 1, French, aminoacide%20catalytiquement%20actif
correct, masculine noun
Record 1, Textual support, French
Record number: 1, Textual support number: 1 CONT
Le chymotrypsinogène est composé d'une chaîne polypeptidique unique contenant 245 acides aminés et comportant cinq liaisons disulfure intracaténaires. Il est transformé en [alpha]-chymotrypsine active par l'hydrolyse enzymatique de quatre liaisons peptidiques sous l'influence séquentielle de la trypsine et de la chymotrypsine, avec libération de deux dipeptides. L'[alpha]-chymotrypsine active ainsi produite est constituée de trois chaînes polypeptidiques maintenues par deux liaisons -S-S. Ainsi, les deux acides aminés spécifiques essentiels à l'activité catalytique, l'histidine en position 57 et la sérine 195, se trouvent dans deux chaînes différentes. Néanmoins, des analyses aux rayons X de la structure tertiaire de la chymotrypsine ont établi directement que ces [...] résidus catalytiques [...] se trouvent en fait très proches l'un de l'autre dans la conformation de l'enzyme natif. 2, record 1, French, - r%C3%A9sidu%20catalytique
Record 1, Spanish
Record 1, Textual support, Spanish
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